Document Detail


Studies of the genetics, function, and kinetic mechanism of TagE, the wall teichoic acid glycosyltransferase in Bacillus subtilis 168.
MedLine Citation:
PMID:  21558268     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The biosynthetic enzymes involved in wall teichoic acid biogenesis in gram-positive bacteria have been the subject of renewed investigation in recent years with the benefit of modern tools of biochemistry and genetics. Nevertheless, there have been only limited investigations into the enzymes that glycosylate wall teichoic acid. Decades-old experiments in the model gram-positive bacterium, Bacillus subtilis 168, using phage-resistant mutants implicated tagE (also called gtaA and rodD) as the gene coding for the wall teichoic acid glycosyltransferase. This study and others have provided only indirect evidence to support a role for TagE in wall teichoic acid glycosylation. In this work, we showed that deletion of tagE resulted in the loss of α-glucose at the C-2 position of glycerol in the poly(glycerol phosphate) polymer backbone. We also reported the first kinetic characterization of pure, recombinant wall teichoic acid glycosyltransferase using clean synthetic substrates. We investigated the substrate specificity of TagE using a wide variety of acceptor substrates and found that the enzyme had a strong kinetic preference for the transfer of glucose from UDP-glucose to glycerol phosphate in polymeric form. Further, we showed that the enzyme recognized its polymeric (and repetitive) substrate with a sequential kinetic mechanism. This work provides direct evidence that TagE is the wall teichoic acid glycosyltransferase in B. subtilis 168 and provides a strong basis for further studies of the mechanism of wall teichoic acid glycosylation, a largely uncharted aspect of wall teichoic acid biogenesis.
Authors:
Sarah E Allison; Michael A D'Elia; Sharif Arar; Mario A Monteiro; Eric D Brown
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2011-05-10
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  286     ISSN:  1083-351X     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2011 Jul 
Date Detail:
Created Date:  2011-07-04     Completed Date:  2011-09-08     Revised Date:  2013-06-30    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  23708-16     Citation Subset:  IM    
Affiliation:
Department of Biochemistry and Biomedical Sciences and the Michael G. DeGroote Institute for Infectious Disease Research, McMaster University, Hamilton, Ontario L8N 3Z5, Canada.
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MeSH Terms
Descriptor/Qualifier:
Bacillus subtilis / enzymology*,  genetics
Bacterial Proteins / chemistry,  genetics,  metabolism*
Cell Wall / enzymology*,  genetics
Glycosylation
Glycosyltransferases / chemistry,  genetics,  metabolism*
Kinetics
Mutation
Teichoic Acids / genetics,  metabolism*
Uridine Diphosphate Glucose / chemistry,  genetics,  metabolism
Grant Support
ID/Acronym/Agency:
MOP-15496//Canadian Institutes of Health Research
Chemical
Reg. No./Substance:
0/Bacterial Proteins; 0/Teichoic Acids; 133-89-1/Uridine Diphosphate Glucose; EC 2.4.-/Glycosyltransferases
Comments/Corrections

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